コーパス検索結果 (1語後でソート)
通し番号をクリックするとPubMedの該当ページを表示します
1 ynureninyl products as well as betaMet-55 to methionine sulfoxide.
2 elding both the (R) and (S) diastereomers of methionine sulfoxide.
3 non-polar methionine to the more hydrophilic methionine sulfoxide.
4 ected SO band at 1025 cm-1 characteristic of methionine sulfoxide.
5 of one of the peptides had been oxidized to methionine sulfoxide.
6 could not grow, in the presence of H2O2 and methionine sulfoxide.
7 yeast strain could grow on either form of L-methionine sulfoxide.
8 on of surface-exposed methionine residues to methionine sulfoxide.
9 ontaining DmsABC enzymatic complex to reduce methionine sulfoxide.
10 ted four out of nine Met residues of RecA to methionine sulfoxide.
11 by phagocytes oxidize methionine, generating methionine sulfoxide.
12 residues are posttranslationally oxidized to methionine sulfoxide.
13 eferentially targeted, forming predominantly methionine sulfoxide.
14 HypT is activated by methionine oxidation to methionine sulfoxide.
15 e reaction, oxidizing methionine residues to methionine sulfoxide.
16 ic oxidation and reduction of methionine and methionine sulfoxide.
17 thionine and is specific for the S epimer of methionine sulfoxide.
18 rrelated and also correlated positively with methionine sulfoxide.
19 ic oxidation and reduction of methionine and methionine sulfoxide.
20 ndogenous methionines to their corresponding methionine sulfoxides.
21 ated CaMox, which varies from three to eight methionine sulfoxides.
22 multiple methionines to their corresponding methionine sulfoxides.
23 r/MsrA mutant could not grow on a mixture of methionine sulfoxides.
24 olysis of methionine gives rise primarily to methionine sulfoxide (+16 Da mass shift); this can be fu
26 d amino acid profile and increased levels of methionine sulfoxide, an oxidative stress biomarker, in
27 ich both methionine residues are oxidized to methionine sulfoxide and a control peptide consisting of
30 rew better, had lower free and protein-bound methionine sulfoxide and had a better survival rate unde
33 shed through mass spectrometric detection of methionine sulfoxide and the reactivation of a significa
35 amino acid methionine is readily oxidized to methionine sulfoxide, and its reduction is catalyzed by
36 malondialdehyde, protein carbonyls, protein methionine sulfoxide, and oxidized glutathione as well a
37 on of microcystins containing methionine and methionine sulfoxide, and reveals the oxidation state of
38 idants react readily with methionine to form methionine sulfoxide, and surface exposed methionine res
39 xygen species oxidize methionine residues to methionine sulfoxide, and the methionine sulfoxide reduc
40 n spectroscopy reveals the presence of H2O2, methionine sulfoxide, and tryptophan metabolites; i.e.,
43 This suggests that microcystins containing methionine sulfoxide are primarily postextraction oxidat
44 ver tissue confirms that both methionine and methionine-sulfoxide are significantly more elevated in
46 to its facile oxidation via the formation of methionine sulfoxide, as shown by mass spectrometry.
47 is demonstrated that oxidation of Met-148 to methionine sulfoxide associated quantitatively with loss
48 the effects of oxidative damage by reducing methionine sulfoxide back to methionine and recovering p
54 n be repaired via reduction of the resulting methionine sulfoxides by methionine-S-sulfoxide reductas
55 susceptible to oxidation, and the resulting methionine sulfoxides can be reduced back to methionines
56 oxidized proteins and MsrA, which reduces S-methionine sulfoxide, can protect lens cells against oxi
57 s are particularly sensitive to oxidation to methionine sulfoxide derivatives, these oxidations are r
59 ification of methionine to the corresponding methionine sulfoxide does not predispose CaM to further
60 n was through the oxidation of methionine to methionine sulfoxide, established through mass spectrome
61 ctivate the PM Ca-ATPase results solely from methionine sulfoxide formation and (ii) MsrA can repair
62 idation of protein-bound methionines to form methionine sulfoxides has a broad range of biological ra
63 e roles of MsrB1, -B2 and -B3 which reduce R-methionine sulfoxide have not been established for any m
65 ctional domains of ADAMTS13 were oxidized to methionine sulfoxide in an HOCl concentration-dependent
67 , except that the myristoylated form reduced methionine sulfoxide in protein much faster than the non
68 e discuss how the oxidation of methionine to methionine sulfoxide in signalling proteins such as ion
69 -Raman Spectroscopy revealed the presence of methionine sulfoxide in the depigmented skin of patients
70 of Bacillus species were readily oxidized to methionine sulfoxide in vitro by t-butyl hydroperoxide (
71 hat MsrA is responsible for the reduction of methionine sulfoxide in vivo as well as in vitro in euka
76 The oxidation of methionine in proteins to methionine sulfoxide is implicated in aging as well as i
77 lysis by reducing agents such as TCEP, while methionine sulfoxide is refractory to reduction by this
78 gments of CaMox vary by a factor of 2, where methionine sulfoxides located within hydrophobic sequenc
79 osition (x = 7, 9, and 11) of methionine (M)/methionine sulfoxide (M-ox) within the peptide sequences
80 that oxidation of the Met-35 side chain to a methionine sulfoxide (Met-35(ox)) significantly hinders
81 ctase (MsrA; EC ) catalyzes the reduction of methionine sulfoxide (Met-O) in proteins to methionine (
82 lot in association with a functional loss of methionine sulfoxide (Met-S=O) repair in the entire gray
84 epair enzyme that catalyzes the reduction of methionine sulfoxide [Met(O)] residues in proteins to me
85 ling, and their reversible oxidation to form methionine sulfoxides [Met(O)] in calmodulin (CaM) and o
91 These latter small peptides are enriched in methionine sulfoxides (MetO), suggesting a preferential
92 e oxygen species (ROS) oxidize methionine to methionine sulfoxide (MetSO) and thereby inactivate prot
93 e oxygen species (ROS) oxidize methionine to methionine sulfoxide (MetSO) and thereby inactivate prot
94 ve developed a new technique for quantifying methionine sulfoxide (MetSO) in protein to assess levels
95 the oxidative stress-induced R enantiomer of methionine sulfoxide (MetSO), reducing it to methionine
97 ies that reduce the S and R stereoisomers of methionine sulfoxide (MetSO), respectively, and together
100 tified the major metabolite, 3-nitrotyrosine-methionine-sulfoxide (NSO)-MENK, using liquid chromatogr
101 mmunosuppressive activity than their reduced methionine sulfoxide peptide forms 4 and 6, respectively
102 loped a sensitive method of quantitating the methionine sulfoxide present at position 213 (MetSO213)
103 r Met(146) in wheat germ calmodulin (CaM) to methionine sulfoxide prevents the CaM-dependent activati
104 commentary shows that both diastereomers of methionine sulfoxide (R and S) can be repaired in the hu
106 these genes are fused to form a bifunctional methionine sulfoxide reductase (i.e., MsrBA) enzyme.
107 enerally accepted, primarily from studies on methionine sulfoxide reductase (Msr) A, that the biologi
110 presses antioxidant enzymes, among which are methionine sulfoxide reductase (Msr) enzymes, which are
112 Met5 of alphaS are excellent substrates for methionine sulfoxide reductase (Msr), thereby providing
119 ty with the carboxyl terminus of the peptide-methionine sulfoxide reductase (MsrA), a repair enzyme,
121 ted by an unrelated protein known as peptide methionine sulfoxide reductase (MsrA), an antioxidant re
122 an mutants in cytochrome c peroxidase (ccp), methionine sulfoxide reductase (msrA), or the metal-bind
123 oxidized alpha/beta-type SASP with peptidyl methionine sulfoxide reductase (MsrA), which can reduce
132 ild-type plants and a mutant lacking peptide methionine sulfoxide reductase (pmsr2-1) showed increase
133 hesin (one UGA) of Mycoplasma pneumoniae and methionine sulfoxide reductase (two UGAs) of Mycoplasma
134 thione peroxidase, ascorbate peroxidase, and methionine sulfoxide reductase 2) are slightly up-regula
135 cardial CaMKII inhibition, overexpression of methionine sulfoxide reductase A (an enzyme that reduces
138 o lower laying rate, egg mass, expression of methionine sulfoxide reductase A (MSRA) gene, and antiox
142 quitously expressed methionine repair enzyme methionine sulfoxide reductase A (MsrA) on the metabolic
144 that a mutant form of M. genitalium lacking methionine sulfoxide reductase A (MsrA), an antioxidant
147 n that can be reversed through the action of methionine sulfoxide reductase A (MsrA), which is implic
148 n-like domain (NT domain) is fused to tandem methionine sulfoxide reductase A and B domains (MsrA/B).
149 r, we demonstrate almost absent catalase and methionine sulfoxide reductase A and B protein expressio
150 horesis (CE) method for the determination of methionine sulfoxide reductase A and methionine sulfoxid
154 have unraveled the redox relay mechanisms of methionine sulfoxide reductase A of the pathogen Coryneb
155 quinone reductase, glutathione reductase and methionine sulfoxide reductase A proteins were significa
156 xpressions of only glutathione reductase and methionine sulfoxide reductase A proteins were significa
157 ecies signaling by targeting the antioxidant methionine sulfoxide reductase A to modulate liposarcoma
158 TARD3 as an in vivo binding partner of MSRA (methionine sulfoxide reductase A), an enzyme that reduce
159 dium-restricted transgenic overexpression of methionine sulfoxide reductase A, an enzyme that reduces
160 dants superoxide dismutase (SOD2), catalase, methionine sulfoxide reductase A, and the 20S proteasome
161 ysine residues of diverse targets, including methionine sulfoxide reductase A, myosin light chain kin
162 whereas over-expression of a repair enzyme, methionine sulfoxide reductase A, rendered them resistan
164 ained by uniform selenium deficiency because methionine sulfoxide reductase activities were similar i
166 tion of methionine sulfoxide reductase A and methionine sulfoxide reductase B activities in mouse liv
167 o binding MSRA, STARD3 binds all three MSRB (methionine sulfoxide reductase B), enzymes that reduce m
170 lly, we found that a cytosolic pool of human methionine sulfoxide reductase B2 (MsrB2) is strongly re
174 ossesses significant homology to the peptide methionine sulfoxide reductase family of enzymes, specif
176 s of apoA-I and oxidized apoA-I treated with methionine sulfoxide reductase implicate oxidation of sp
178 ding or the repair of oxidized calmodulin by methionine sulfoxide reductase induces comparable change
179 e pK(a) of the active site cysteine of mouse methionine sulfoxide reductase is 7.2 even in the absenc
180 of oxidized methionine residues performed by methionine sulfoxide reductase is important for the gast
181 versible and is regulated by the cytoplasmic methionine sulfoxide reductase Mxr1 (MsrA) and a previou
185 ine in proteins involving the enzyme peptide methionine sulfoxide reductase type A (MSRA) is postulat
186 m Escherichia coli and the electron acceptor methionine sulfoxide reductase, also from E. coli, stron
196 nt study on the reducing requirement for the methionine sulfoxide reductases (Msr), we have shown tha
202 s damage is reversible through the action of methionine sulfoxide reductases (MSRs), which play key r
206 revisiae as a model, we show that of the two methionine sulfoxide reductases (MXR1, MXR2), deletion o
207 rx2) and the intracellular and extracellular methionine sulfoxide reductases (SpMsrAB1 and SpMsrAB2,
208 (MetO) residues in proteins is catalyzed by methionine sulfoxide reductases A (MSRA) and B (MSRB), w
210 S) can be repaired in the human epidermis by methionine sulfoxide reductases A and B, respectively.
216 ne residues to methionine sulfoxide, and the methionine sulfoxide reductases catalyze their reduction
217 activity of plastidial thiol peroxidases and methionine sulfoxide reductases employing a single cyste
218 a proof of principle, fluorogenic probes for methionine sulfoxide reductases have been developed.
222 teins or repair oxidized residues, including methionine sulfoxide reductases MsrA and MsrB, which red
225 sporadically evolved Sec-containing forms of methionine sulfoxide reductases reflect catalytic advant
234 rved SelR enzyme family, define a pathway of methionine sulfoxide reduction, reveal a case of converg
237 sulfoxide reductase (MsrA), which can reduce methionine sulfoxide residues back to methionine, restor
238 4.6) is a ubiquitous protein that can reduce methionine sulfoxide residues in proteins as well as in
239 fense against oxidative stresses by reducing methionine sulfoxide residues in proteins back to methio
240 MsrA and MsrB in E. coli are able to reduce methionine sulfoxide residues in proteins to methionines
244 24) thiolate, which directly interacted with methionine sulfoxide, resulting in methionine and a Cys(
245 oxide reductases A and B specifically reduce methionine sulfoxides (S) and (R), respectively, back to
246 activity and the reduction activity of free methionine sulfoxide(s) were stereoselective toward the
248 usly unrecognized part that accommodates the methionine sulfoxide side chain via interaction with His
249 ous substitution by glutamine, mimicking the methionine sulfoxide state, increased the viability of E
250 ge into methionine, N-glycyl-methionine, and methionine sulfoxide suggests that a prominent solvent e
251 )H incorporation into the gamma-methylene of methionine sulfoxide that is absent for N-glycyl-methion
253 nonoxidized), and with increasing numbers of methionine sulfoxides the kinetics of fibrillation becam
254 When this methionine residue is oxidized to methionine sulfoxide, the inactivation is disrupted, and
255 tein repair each targeting a diastereomer of methionine sulfoxide, their deletion resulted in differe
256 ble to oxidation with a 25-75% loss, forming methionine sulfoxide through a two-electron oxidation pa
257 with methionine residues in proteins to form methionine sulfoxide, thus scavenging the reactive speci
258 eductase A (MsrA) catalyzes the reduction of methionine sulfoxide to methionine and is specific for t
259 ethionine sulfoxide reductase, which reduces methionine sulfoxide to methionine in a thioredoxin-depe
260 Taken together, MSRB3-catalyzed reduction of methionine sulfoxides to methionine is essential for hea
261 so capable of reducing nicotinamide N-oxide, methionine sulfoxide, trimethylamine-N-oxide, and dimeth
263 rmore, high levels of free and protein-bound methionine sulfoxide were detected in extracts of msrA m
264 metformin therapy, arginine-derived AGE and methionine sulfoxide were lower than in patients not rec
265 -Glu-cys, gamma-Glu-met-gly, methionine, and methionine sulfoxide were not transported by Seo1p.
266 markers of oxidative stress such as urinary methionine sulfoxide were observed in Hhip (+/-) but not
267 of a variety of other substrates, including methionine sulfoxide, with decreased efficiencies, sugge
269 air by MsrA, there remains a distribution of methionine sulfoxides within functionally reactivated Ca
271 dary structure, suggesting that MsrA repairs methionine sulfoxides within unfolded sequences until na
272 e report the synthesis of amphiphilic poly(l-methionine sulfoxide)(x)-b-poly(dehydroalanine)(y), dibl